메뉴 건너뛰기




Volumn 73, Issue 7, 2014, Pages 693-701

Lack of neuropathy-related phenotypes in Hint1 knockout mice

Author keywords

Animal model; Axon degeneration; Charcot Marie Tooth disease; HINT1; Histidine triad nucleotide binding protein 1; Neuromyotonia

Indexed keywords

3,4 DIAMINOPYRIDINE; HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEIN 1; NUCLEOTIDE BINDING PROTEIN; POTASSIUM CHANNEL; UNCLASSIFIED DRUG;

EID: 84903265318     PISSN: 00223069     EISSN: 15546578     Source Type: Journal    
DOI: 10.1097/NEN.0000000000000085     Document Type: Article
Times cited : (25)

References (31)
  • 2
    • 0028124225 scopus 로고
    • Episodic ataxia/myokymia syndrome is associated with point mutations in the human potassium channel gene, KCNA1
    • Browne DL, Gancher ST, Nutt JG, et al. Episodic ataxia/myokymia syndrome is associated with point mutations in the human potassium channel gene, KCNA1. Nat Gen 1994;8:136-40
    • (1994) Nat Gen , vol.8 , pp. 136-140
    • Browne, D.L.1    Gancher, S.T.2    Nutt, J.G.3
  • 3
    • 84866840027 scopus 로고    scopus 로고
    • Loss-of-function mutations in HINT1 cause axonal neuropathy with neuromyotonia
    • Zimon M, Baets J, Almeida-Souza L, et al. Loss-of-function mutations in HINT1 cause axonal neuropathy with neuromyotonia. Nat Gen 2012;44: 1080-83
    • (2012) Nat Gen , vol.44 , pp. 1080-1083
    • Zimon, M.1    Baets, J.2    Almeida-Souza, L.3
  • 4
    • 84891593253 scopus 로고    scopus 로고
    • Autosomal recessive axonal neuropathy with neuromyotonia: A rare entity
    • Caetano JS, Costa C, Baets J, et al. Autosomal recessive axonal neuropathy with neuromyotonia: A rare entity. Pediatr Neurol 2014;50: 104-7
    • (2014) Pediatr Neurol , vol.50 , pp. 104-107
    • Caetano, J.S.1    Costa, C.2    Baets, J.3
  • 5
    • 84901035232 scopus 로고    scopus 로고
    • Exome sequencing reveals HINT1 mutations as a cause of distal hereditary motor neuropathy [published online ahead of print October 9 2013]
    • doi: 10.1038/ejhg.2013.231
    • Zhao H, Race V, Matthijs G, et al. Exome sequencing reveals HINT1 mutations as a cause of distal hereditary motor neuropathy [published online ahead of print October 9, 2013]. Eur J Hum Gen. doi: 10.1038/ejhg.2013.231.
    • Eur J Hum Gen
    • Zhao, H.1    Race, V.2    Matthijs, G.3
  • 7
    • 0037934419 scopus 로고    scopus 로고
    • Deletion of histidine triad nucleotide-binding protein 1/PKC-interacting protein in mice enhances cell growth and carcinogenesis
    • Su T, Suzui M, Wang L, et al. Deletion of histidine triad nucleotide-binding protein 1/PKC-interacting protein in mice enhances cell growth and carcinogenesis. Proc Natl Acad Sci USA 2003;100: 7824-29
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7824-7829
    • Su, T.1    Suzui, M.2    Wang, L.3
  • 8
    • 32244448801 scopus 로고    scopus 로고
    • Hint1 is a haplo-insufficient tumor suppressor in mice
    • Li H, Zhang Y, Su T, et al. Hint1 is a haplo-insufficient tumor suppressor in mice. Oncogene 2006;25:713-21
    • (2006) Oncogene , vol.25 , pp. 713-721
    • Li, H.1    Zhang, Y.2    Su, T.3
  • 9
    • 0039613985 scopus 로고    scopus 로고
    • Suppression of microphthalmia transcriptional activity by its association with protein kinase CYinteracting protein 1 in mast cells
    • Razin E, Zhang ZC, Nechushtan H, et al. Suppression of microphthalmia transcriptional activity by its association with protein kinase CYinteracting protein 1 in mast cells. J Biol Chem 1999;274:34272-76
    • (1999) J Biol Chem , vol.274 , pp. 34272-34276
    • Razin, E.1    Zhang, Z.C.2    Nechushtan, H.3
  • 10
    • 84878639592 scopus 로고    scopus 로고
    • Histidine triad nucleotide-binding protein 1 (HINT1) regulates Ca(2+) signaling in mouse fibroblasts and neuronal cells via store-operated Ca(2+) entry pathway
    • Linde CI, Feng B, Wang JB, et al. Histidine triad nucleotide-binding protein 1 (HINT1) regulates Ca(2+) signaling in mouse fibroblasts and neuronal cells via store-operated Ca(2+) entry pathway. Am J Physiol Cell Physiol 2013;304:C1098-104
    • (2013) Am J Physiol Cell Physiol , vol.304
    • Linde, C.I.1    Feng, B.2    Wang, J.B.3
  • 11
    • 0020169938 scopus 로고
    • Mechanism of synthesis of adenosine(5¶)tetraphospho(5¶) adenosine (AppppA) by aminoacyl-tRNA synthetases
    • Goerlich O, Foeckler R, Holler E. Mechanism of synthesis of adenosine(5¶)tetraphospho(5¶)adenosine (AppppA) by aminoacyl-tRNA synthetases. Eur J Biochem 1982;126:135-42
    • (1982) Eur J Biochem , vol.126 , pp. 135-142
    • Goerlich, O.1    Foeckler, R.2    Holler, E.3
  • 12
    • 0038067742 scopus 로고    scopus 로고
    • Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type v
    • Antonellis A, Ellsworth RE, Sambuughin N, et al. Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V. Am J Hum Gen 2003;72:1293-99
    • (2003) Am J Hum Gen , vol.72 , pp. 1293-1299
    • Antonellis, A.1    Ellsworth, R.E.2    Sambuughin, N.3
  • 13
    • 31744448271 scopus 로고    scopus 로고
    • Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy
    • Jordanova A, Irobi J, Thomas FP, et al. Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat Genet 2006;38:197-202
    • (2006) Nat Genet , vol.38 , pp. 197-202
    • Jordanova, A.1    Irobi, J.2    Thomas, F.P.3
  • 14
    • 73349114324 scopus 로고    scopus 로고
    • A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease
    • Latour P, Thauvin-Robinet C, Baudelet-Mery C, et al. A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. Am J Hum Gen 2010;86:77-82
    • (2010) Am J Hum Gen , vol.86 , pp. 77-82
    • Latour, P.1    Thauvin-Robinet, C.2    Baudelet-Mery, C.3
  • 15
    • 33748545328 scopus 로고    scopus 로고
    • An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model
    • Seburn KL, Nangle LA, Cox GA, et al. An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model. Neuron 2006;51:715-26
    • (2006) Neuron , vol.51 , pp. 715-726
    • Seburn, K.L.1    Nangle, L.A.2    Cox, G.A.3
  • 16
    • 21444451106 scopus 로고    scopus 로고
    • Gait analysis detects early changes in transgenic SOD1(G93A) mice
    • Wooley CM, Sher RB, Kale A, et al. Gait analysis detects early changes in transgenic SOD1(G93A) mice. Muscle Nerve 2005;32:43-50
    • (2005) Muscle Nerve , vol.32 , pp. 43-50
    • Wooley, C.M.1    Sher, R.B.2    Kale, A.3
  • 17
    • 58149520161 scopus 로고    scopus 로고
    • Age, experience and genetic background influence treadmill walking in mice
    • Wooley CM, Xing S, Burgess RW, et al. Age, experience and genetic background influence treadmill walking in mice. Physiol Behav 2009;96: 350-61
    • (2009) Physiol Behav , vol.96 , pp. 350-361
    • Wooley, C.M.1    Xing, S.2    Burgess, R.W.3
  • 19
    • 84855289563 scopus 로고    scopus 로고
    • Charcot-Marie-ToothYlinked mutant GARS is toxic to peripheral neurons independent of wild-type GARS levels
    • Motley WW, Seburn KL, Nawaz MH, et al. Charcot-Marie-ToothYlinked mutant GARS is toxic to peripheral neurons independent of wild-type GARS levels. PLoS Gen 2011;7:e1002399
    • (2011) PLoS Gen , vol.7
    • Motley, W.W.1    Seburn, K.L.2    Nawaz, M.H.3
  • 20
    • 79953283718 scopus 로고    scopus 로고
    • Increased anxiety-related behaviour in Hint1 knockout mice
    • Varadarajulu J, LebarM, Krishnamoorthy G, et al. Increased anxiety-related behaviour in Hint1 knockout mice. Behav Brain Res 2011;220:305-11
    • (2011) Behav Brain Res , vol.220 , pp. 305-311
    • Varadarajulu, J.1    Lebarm Krishnamoorthy, G.2
  • 21
    • 70349773389 scopus 로고    scopus 로고
    • An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy
    • Achilli F, Bros-Facer V, Williams HP, et al. An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy. Dis Models Mech 2009;2:359-73
    • (2009) Dis Models Mech , vol.2 , pp. 359-373
    • Achilli, F.1    Bros-Facer, V.2    Williams, H.P.3
  • 22
    • 0030724815 scopus 로고    scopus 로고
    • Hereditary neuromyotonia: A mouse model associated with deficiency or increased gene dosage of the PMP22 gene
    • Toyka KV, Zielasek J, Ricker K, et al. Hereditary neuromyotonia: A mouse model associated with deficiency or increased gene dosage of the PMP22 gene. J Neurol Neurosurg Psychiatry 1997;63:812-13
    • (1997) J Neurol Neurosurg Psychiatry , vol.63 , pp. 812-813
    • Toyka, K.V.1    Zielasek, J.2    Ricker, K.3
  • 23
    • 0033554303 scopus 로고    scopus 로고
    • Nerve conduction abnormalities and neuromyotonia in genetically engineered mouse models of human hereditary neuropathies
    • Zielasek J, Toyka KV. Nerve conduction abnormalities and neuromyotonia in genetically engineered mouse models of human hereditary neuropathies. Ann NY Acad Sci 1999;883:310-20
    • (1999) Ann NY Acad Sci , vol.883 , pp. 310-320
    • Zielasek, J.1    Toyka, K.V.2
  • 24
    • 0034020892 scopus 로고    scopus 로고
    • Neuromyotonia in mice with hereditary myelinopathies
    • Zielasek J, Martini R, Suter U, et al. Neuromyotonia in mice with hereditary myelinopathies. Muscle Nerve 2000;23:696-701
    • (2000) Muscle Nerve , vol.23 , pp. 696-701
    • Zielasek, J.1    Martini, R.2    Suter, U.3
  • 25
    • 46249110939 scopus 로고    scopus 로고
    • A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination
    • Patton BL, Wang B, Tarumi YS, et al. A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination. J Cell Sci 2008;121:1593-604
    • (2008) J Cell Sci , vol.121 , pp. 1593-1604
    • Patton, B.L.1    Wang, B.2    Tarumi, Y.S.3
  • 26
    • 0028882747 scopus 로고
    • Acquired neuromyotonia: Evidence for autoantibodies directed against K+ channels of peripheral nerves
    • Shillito P, Molenaar PC, Vincent A, et al. Acquired neuromyotonia: Evidence for autoantibodies directed against K+ channels of peripheral nerves. Ann Neurol 1995;38:714-22
    • (1995) Ann Neurol , vol.38 , pp. 714-722
    • Shillito, P.1    Molenaar, P.C.2    Vincent, A.3
  • 27
    • 84862128116 scopus 로고    scopus 로고
    • Kv1.1 knock-in ataxic mice exhibit spontaneous myokymic activity exacerbated by fatigue, ischemia and low temperature
    • Brunetti O, Imbrici P, Botti FM, et al. Kv1.1 knock-in ataxic mice exhibit spontaneous myokymic activity exacerbated by fatigue, ischemia and low temperature. Neurobiol Dis 2012;47:310-21
    • (2012) Neurobiol Dis , vol.47 , pp. 310-321
    • Brunetti, O.1    Imbrici, P.2    Botti, F.M.3
  • 28
    • 84860261116 scopus 로고    scopus 로고
    • A mouse model of Schwartz-Jampel syndrome reveals myelinating Schwann cell dysfunction with persistent axonal depolarization in vitro and distal peripheral nerve hyperexcitability when perlecan is lacking
    • Bangratz M, Sarrazin N, Devaux J, et al. A mouse model of Schwartz-Jampel syndrome reveals myelinating Schwann cell dysfunction with persistent axonal depolarization in vitro and distal peripheral nerve hyperexcitability when perlecan is lacking. Am J Pathol 2012;180: 2040-55
    • (2012) Am J Pathol , vol.180 , pp. 2040-2055
    • Bangratz, M.1    Sarrazin, N.2    Devaux, J.3
  • 29
    • 53449089265 scopus 로고    scopus 로고
    • Evidence of a dosage effect and a physiological endplate acetylcholinesterase deficiency in the first mouse models mimicking Schwartz-Jampel syndrome neuromyotonia
    • Stum M, Girard E, Bangratz M, et al. Evidence of a dosage effect and a physiological endplate acetylcholinesterase deficiency in the first mouse models mimicking Schwartz-Jampel syndrome neuromyotonia. Hum Mol Gen 2008;17:3166-79
    • (2008) Hum Mol Gen , vol.17 , pp. 3166-3179
    • Stum, M.1    Girard, E.2    Bangratz, M.3
  • 30
    • 84862303538 scopus 로고    scopus 로고
    • Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor.
    • Wang J, Fang P, Schimmel P, et al. Side chain independent recognition of aminoacyl adenylates by the Hint1 transcription suppressor. J Phys Chem B 2012;116:6798-805
    • (2012) J Phys Chem B , vol.116 , pp. 6798-6805
    • Wang, J.1    Fang, P.2    Schimmel, P.3
  • 31
    • 0037192795 scopus 로고    scopus 로고
    • Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3
    • Bieganowski P, Garrison PN, Hodawadekar SC, et al. Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. J Biol Chem 2002;277:10852-60
    • (2002) J Biol Chem , vol.277 , pp. 10852-10860
    • Bieganowski, P.1    Garrison, P.N.2    Hodawadekar, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.